ID A0A670KCI1_PODMU Unreviewed; 812 AA.
AC A0A670KCI1;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 18-JUN-2025, entry version 21.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=RNF19A {ECO:0000313|Ensembl:ENSPMRP00000032537.1};
OS Podarcis muralis (Wall lizard) (Lacerta muralis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Laterata;
OC Lacertibaenia; Lacertidae; Podarcis.
OX NCBI_TaxID=64176 {ECO:0000313|Ensembl:ENSPMRP00000032537.1, ECO:0000313|Proteomes:UP000472272};
RN [1] {ECO:0000313|Ensembl:ENSPMRP00000032537.1, ECO:0000313|Proteomes:UP000472272}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30819892; DOI=10.1073/pnas.1820320116;
RA Andrade P., Pinho C., Perez I de Lanuza G., Afonso S., Brejcha J.,
RA Rubin C.J., Wallerman O., Pereira P., Sabatino S.J., Bellati A.,
RA Pellitteri-Rosa D., Bosakova Z., Bunikis I., Carretero M.A., Feiner N.,
RA Marsik P., Pauperio F., Salvi D., Soler L., While G.M., Uller T., Font E.,
RA Andersson L., Carneiro M.;
RT "Regulatory changes in pterin and carotenoid genes underlie balanced color
RT polymorphisms in the wall lizard.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:5633-5642(2019).
RN [2] {ECO:0000313|Ensembl:ENSPMRP00000032537.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the RBR family. RNF19 subfamily.
CC {ECO:0000256|ARBA:ARBA00061087}.
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DR RefSeq; XP_028592217.1; XM_028736384.1.
DR RefSeq; XP_028592218.1; XM_028736385.1.
DR RefSeq; XP_028592219.1; XM_028736386.1.
DR RefSeq; XP_028592220.1; XM_028736387.1.
DR RefSeq; XP_028592221.1; XM_028736388.1.
DR AlphaFoldDB; A0A670KCI1; -.
DR Ensembl; ENSPMRT00000034501.1; ENSPMRP00000032537.1; ENSPMRG00000021080.1.
DR GeneID; 114600370; -.
DR GeneTree; ENSGT00940000158703; -.
DR OMA; HQCSISL; -.
DR OrthoDB; 1431934at2759; -.
DR Proteomes; UP000472272; Chromosome 7.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20362; BRcat_RBR_RNF19A; 1.
DR CDD; cd20355; Rcat_RBR_RNF19; 1.
DR CDD; cd16775; RING-HC_RBR_RNF19A; 1.
DR FunFam; 1.20.120.1750:FF:000001; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 2.20.25.20:FF:000004; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000052; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 2.20.25.20; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 2.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000472272};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 335..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 388..421
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 102..325
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 106..154
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 10..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..29
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..618
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..690
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 812 AA; 87601 MW; 032380624C3FE11C CRC64;
MNVLAMSLHR QMGSDRDLQS SASSVSLPSI KKAPKKRRIS LGSLFRRKRD TKRKSRDING
GVDGIASIES IHSEMCMDKN SIFSAYMSSD NGTTIISKQS GDFMECPLCL LRHSKERFPE
IMTCHHRSCV DCLRQYLRIE ISESRVNISC PECSERFNPH DIRLILNDDI LMEKYEEFML
RRWLVADPDC RWCPAPDCGY AVIAFGCASC PKLTCGREGC GTEFCYHCKQ IWHPNQTCDA
ARQERAQSLR LRTIRSSSIS YSQESGAAAD DIKPCPRCAA YIIKMNDGSC NHMTCAVCGC
EFCWLCMKEI SDLHYLSPSG CTFWGKKPWS RKKKILWQLG TLVGAPVGIA LIAGIAIPAM
IIGIPVYVGR KIHNRYEGKD ISKHKRNLAI AGGVTLSVIV SPVVAAVTVG IGVPIMLAYV
YGVVPISLCR SGGCGVSAGN GKGVRIEFDD ENDITVGGTN AAVDTTSVAE ARNNPSIGEE
SVGGLTGSLS ASGSHMDRMG AIRDNLSETA STMALAGASI TGSLSGSAMV NCFNRLEVQA
DVQKERCSLS GESGTVSLGT VSDNASTKAM AGSILNSYIP LDRDSSSMEV QVDIESKPTK
FRHNSGSSSV DDGSSAGQSN AGCSSACLSE NKSSATKWSK DASAGKKCKG KLRKKSSMKI
NETREDMDAQ LLEQQSTNSS EFDSPSLSDS IPSVADSHSS HFSEFSCSDM ESMKTSCSHG
SSDYHTRFTT VNILPEVEND RLENSPHQSG NSLLIPAAPN SEAPQLSYIA EECVYNGTSG
VADVGTGETL KEANNNHSQH AVELNAAIQT EI
//
